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Patterns of Amino Acids near Signal‐Sequence Cleavage Sites

European Journal of Biochemistry · 1983 · Vol. 133(1) · pp. 17–21
Gunnar von Heijne

Abstract

According to the signal hypothesis, a signal sequence, once having initiated export of a growing protein chain across the rough endoplasmic reticulum, is cleaved from the mature protein at a specific site. It has long been known that some part of the cleavage specificity resides in the last residue of the signal sequence, which invariably is one with a small, uncharged side-chain, but no further specific patterns of amino acids near the point of cleavage have been discovered so far. In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.

Protein Structure and DynamicsMachine Learning in BioinformaticsRNA and protein synthesis mechanismsCleavage (geology)Signal peptideSignal peptidaseEndoplasmic reticulumProtein Sorting SignalsAmino acidSequence (biology)SIGNAL (programming language)Cleavage factorProtein sequencing

MeSH terms

Amino Acid SequenceAnimalsBinding SitesEukaryotic CellsHumansPeptide Chain Termination, Translational
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Empirical Predictions of Protein Conformation
Annual Review of Biochemistry · 1978 · 3,142 citations
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